Abstract

The family of 2,3-aminomutases catalyzes the migration of an amine group from the α-carbon to the β-carbon of l-arylalanines. The first 4-methylideneimidazole-5-one (MIO)-containing aminomutase was discovered in 2003, catalyzing (S)-β-tyrosine formation in the biosynthesis of the enediyne C-1027 and sharing homology with the well-studied ammonia lyases. Since then, several MIO-containing aminomutases have been characterized, catalyzing the formation of varying β-arylalanines in the biosynthesis of Taxol, kedarcidin, and other natural products.

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